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Protein

Peroxiredoxin-1

Gene

Prdx1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity).By similarity

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei52 – 521Cysteine sulfenic acid (-SOH) intermediate

GO - Molecular functioni

  • heme binding Source: RGD
  • peroxidase activity Source: UniProtKB-KW
  • peroxiredoxin activity Source: RGD
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • cellular oxidant detoxification Source: GOC
  • response to oxidative stress Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BRENDAi1.11.1.15. 5301.
ReactomeiR-RNO-3299685. Detoxification of Reactive Oxygen Species.
R-RNO-5628897. TP53 Regulates Metabolic Genes.

Protein family/group databases

PeroxiBasei4508. Rno2CysPrx01.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-1 (EC:1.11.1.15)
Alternative name(s):
HBP23
Heme-binding 23 kDa protein
Thioredoxin peroxidase 2
Thioredoxin-dependent peroxide reductase 2
Gene namesi
Name:Prdx1
Synonyms:Tdpx2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi620039. Prdx1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • melanosome Source: UniProtKB-SubCell
  • mitochondrial matrix Source: RGD
  • nuclear euchromatin Source: RGD
  • nucleolus Source: RGD
  • peroxisomal matrix Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 199198Peroxiredoxin-1PRO_0000135078Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei7 – 71N6-acetyllysineBy similarity
Modified residuei16 – 161N6-acetyllysineBy similarity
Modified residuei27 – 271N6-acetyllysineBy similarity
Modified residuei32 – 321PhosphoserineBy similarity
Modified residuei35 – 351N6-acetyllysine; alternateBy similarity
Modified residuei35 – 351N6-succinyllysine; alternateBy similarity
Disulfide bondi52 – 52Interchain (with C-173); in linked form
Modified residuei90 – 901PhosphothreonineBy similarity
Modified residuei136 – 1361N6-acetyllysineBy similarity
Disulfide bondi173 – 173Interchain (with C-52); in linked form

Post-translational modificationi

Phosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic activity.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiQ63716.
PRIDEiQ63716.

2D gel databases

World-2DPAGE0004:Q63716.

PTM databases

iPTMnetiQ63716.
PhosphoSiteiQ63716.
SwissPalmiQ63716.

Expressioni

Gene expression databases

GenevisibleiQ63716. RN.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation. May form heterodimers with AOP2. Interacts with GDPD5; forms a mixed-disulfide with GDPD5 (By similarity).By similarity

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi250701. 3 interactions.
IntActiQ63716. 4 interactions.
STRINGi10116.ENSRNOP00000023132.

Structurei

Secondary structure

1
199
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 205Combined sources
Beta strandi26 – 305Combined sources
Helixi31 – 344Combined sources
Beta strandi37 – 437Combined sources
Beta strandi50 – 523Combined sources
Helixi57 – 615Combined sources
Helixi63 – 686Combined sources
Beta strandi71 – 788Combined sources
Helixi81 – 888Combined sources
Helixi92 – 943Combined sources
Beta strandi104 – 1063Combined sources
Helixi111 – 1155Combined sources
Beta strandi121 – 1244Combined sources
Beta strandi128 – 1336Combined sources
Beta strandi137 – 1459Combined sources
Helixi153 – 16816Combined sources
Beta strandi170 – 1723Combined sources
Turni188 – 1914Combined sources
Helixi192 – 1954Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QQ2X-ray2.60A/B1-199[»]
2Z9SX-ray2.90A/B/C/D/E/F/G/H/I/J1-199[»]
ProteinModelPortaliQ63716.
SMRiQ63716. Positions 3-199.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ63716.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 165160ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the AhpC/TSA family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiQ63716.
KOiK13279.
OMAiEFKKINC.
OrthoDBiEOG7T1RCD.
PhylomeDBiQ63716.
TreeFamiTF105181.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q63716-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSGNAKIGH PAPSFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF
60 70 80 90 100
VCPTEIIAFS DRAEEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM
110 120 130 140 150
NIPLVSDPKR TIAQDYGVLK ADEGISFRGL FIIDDKGILR QITINDLPVG
160 170 180 190
RSVDEILRLV QAFQFTDKHG EVCPAGWKPG SDTIKPDVNK SKEYFSKQK
Length:199
Mass (Da):22,109
Last modified:November 1, 1996 - v1
Checksum:iBDF2D4ABA8A776DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30035 mRNA. Translation: BAA06275.1.
BC058450 mRNA. Translation: AAH58450.1.
BC088118 mRNA. Translation: AAH88118.1.
PIRiI52425.
RefSeqiNP_476455.1. NM_057114.1.
UniGeneiRn.2845.

Genome annotation databases

EnsembliENSRNOT00000023132; ENSRNOP00000023132; ENSRNOG00000017194.
GeneIDi117254.
KEGGirno:117254.
UCSCiRGD:620039. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D30035 mRNA. Translation: BAA06275.1.
BC058450 mRNA. Translation: AAH58450.1.
BC088118 mRNA. Translation: AAH88118.1.
PIRiI52425.
RefSeqiNP_476455.1. NM_057114.1.
UniGeneiRn.2845.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QQ2X-ray2.60A/B1-199[»]
2Z9SX-ray2.90A/B/C/D/E/F/G/H/I/J1-199[»]
ProteinModelPortaliQ63716.
SMRiQ63716. Positions 3-199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250701. 3 interactions.
IntActiQ63716. 4 interactions.
STRINGi10116.ENSRNOP00000023132.

Protein family/group databases

PeroxiBasei4508. Rno2CysPrx01.

PTM databases

iPTMnetiQ63716.
PhosphoSiteiQ63716.
SwissPalmiQ63716.

2D gel databases

World-2DPAGE0004:Q63716.

Proteomic databases

PaxDbiQ63716.
PRIDEiQ63716.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000023132; ENSRNOP00000023132; ENSRNOG00000017194.
GeneIDi117254.
KEGGirno:117254.
UCSCiRGD:620039. rat.

Organism-specific databases

CTDi5052.
RGDi620039. Prdx1.

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiQ63716.
KOiK13279.
OMAiEFKKINC.
OrthoDBiEOG7T1RCD.
PhylomeDBiQ63716.
TreeFamiTF105181.

Enzyme and pathway databases

BRENDAi1.11.1.15. 5301.
ReactomeiR-RNO-3299685. Detoxification of Reactive Oxygen Species.
R-RNO-5628897. TP53 Regulates Metabolic Genes.

Miscellaneous databases

EvolutionaryTraceiQ63716.
PROiQ63716.

Gene expression databases

GenevisibleiQ63716. RN.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Purification, characterization, and cloning of a heme-binding protein (23 kDa) in rat liver cytosol."
    Iwahara S., Satoh H., Song D.-X., Webb J., Burlingame A.L., Nagae Y., Mueller-Eberhard U.
    Biochemistry 34:13398-13406(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver and Pituitary.
  3. Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 17-35 AND 111-190, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  4. "Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product."
    Hirotsu S., Abe Y., Okada K., Nagahara N., Hori H., Nishino T., Hakoshima T.
    Proc. Natl. Acad. Sci. U.S.A. 96:12333-12338(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN OXIDIZED FORM.

Entry informationi

Entry nameiPRDX1_RAT
AccessioniPrimary (citable) accession number: Q63716
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is the redox-active Cys-52 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin.
Inactivated upon oxidative stress by overoxidation of Cys-52 to Cys-SO2H and Cys-SO3H. Cys-SO2H is retroreduced to Cys-SOH after removal of H2O2, while Cys-SO3H may be irreversibly oxidized.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.